CYP2W1
Description
The CYP2W1 (cytochrome P450 family 2 subfamily W member 1) is a protein-coding gene located on chromosome 7.
CYP2W1 (cytochrome P450, family 2, subfamily W, polypeptide 1) is a protein encoded by the CYP2W1 gene in humans. It belongs to the cytochrome P450 superfamily of enzymes, which are monooxygenases involved in drug metabolism and the synthesis of cholesterol, steroids, and other lipids. CYP2W1 is unique because it is primarily expressed in tumors and not in normal human tissue.
CYP2W1 is a cytochrome P450 monooxygenase that plays a role in retinoid and phospholipid metabolism. It catalyzes the hydroxylation of saturated carbon hydrogen bonds and hydroxylates all-trans retinoic acid (atRA) to 4-hydroxyretinoate, potentially regulating atRA clearance. Other retinoids like all-trans retinol and all-trans retinal are potential endogenous substrates. It also catalyzes both epoxidation of double bonds and hydroxylation of carbon hydrogen bonds of the fatty acyl chain of 1-acylphospholipids/2-lysophospholipids. CYP2W1 can metabolize various lysophospholipid classes, including lysophosphatidylcholines (LPCs), lysophosphatidylinositols (LPIs), lysophosphatidylserines (LPSs), lysophosphatidylglycerols (LPGs), lysophosphatidylethanolamines (LPEs), and lysophosphatidic acids (LPAs). It has low or no activity towards 2-acylphospholipids/1-lysophospholipids, diacylphospholipids, and free fatty acids. Additionally, CYP2W1 may contribute to tumorigenesis by activating procarcinogens like aflatoxin B1, polycyclic aromatic hydrocarbon dihydrodiols, and aromatic amines. Mechanistically, it uses molecular oxygen, inserting one oxygen atom into a substrate and reducing the second into a water molecule. Two electrons are provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
CYP2W1 is also known as -.
